2rjk: Difference between revisions
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==Crystal Structure of Human TL1A Extracellular Domain C95S Mutant== | ==Crystal Structure of Human TL1A Extracellular Domain C95S Mutant== | ||
<StructureSection load='2rjk' size='340' side='right' caption='[[2rjk]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2rjk' size='340' side='right'caption='[[2rjk]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2rjk]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2rjk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RJK FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qe3|2qe3]], [[2rjl|2rjl]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qe3|2qe3]], [[2rjl|2rjl]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TNFSF15 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TNFSF15 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rjk OCA], [https://pdbe.org/2rjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rjk RCSB], [https://www.ebi.ac.uk/pdbsum/2rjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rjk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/TNF15_HUMAN TNF15_HUMAN]] Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis.<ref>PMID:9872942</ref> <ref>PMID:11923219</ref> <ref>PMID:11911831</ref> <ref>PMID:10597252</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Tumor necrosis factor ligand superfamily|Tumor necrosis factor ligand superfamily]] | *[[Tumor necrosis factor ligand superfamily 3D structures|Tumor necrosis factor ligand superfamily 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | |||
[[Category: Almo, S C]] | [[Category: Almo, S C]] | ||
[[Category: Bonanno, J]] | [[Category: Bonanno, J]] | ||
Revision as of 07:27, 2 July 2021
Crystal Structure of Human TL1A Extracellular Domain C95S MutantCrystal Structure of Human TL1A Extracellular Domain C95S Mutant
Structural highlights
Function[TNF15_HUMAN] Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis.[1] [2] [3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTNF-like 1A (TL1A) is a newly described member of the TNF superfamily that is directly implicated in the pathogenesis of autoimmune diseases, including inflammatory bowel disease, atherosclerosis, and rheumatoid arthritis. We report the crystal structure of the human TL1A extracellular domain at a resolution of 2.5 A, which reveals a jelly-roll fold typical of the TNF superfamily. This structural information, in combination with complementary mutagenesis and biochemical characterization, provides insights into the binding interface and the specificity of the interactions between TL1A and the DcR3 and DR3 receptors. These studies suggest that the mode of interaction between TL1A and DcR3 differs from other characterized TNF ligand/receptor complexes. In addition, we have generated functional TL1A mutants with altered disulfide bonding capability that exhibit enhanced solution properties, which will facilitate the production of materials for future cell-based and whole animal studies. In summary, these studies provide insights into the structure and function of TL1A and provide the basis for the rational manipulation of its interactions with cognate receptors. Biochemical and structural characterization of the human TL1A ectodomain.,Zhan C, Yan Q, Patskovsky Y, Li Z, Toro R, Meyer A, Cheng H, Brenowitz M, Nathenson SG, Almo SC Biochemistry. 2009 Aug 18;48(32):7636-45. PMID:19522538[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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